PrkA controls peptidoglycan biosynthesis through the essential phosphorylation of ReoM.

Abstract:

:Peptidoglycan (PG) is the main component of bacterial cell walls and the target for many antibiotics. PG biosynthesis is tightly coordinated with cell wall growth and turnover, and many of these control activities depend upon PASTA-domain containing eukaryotic-like serine/threonine protein kinases (PASTA-eSTK) that sense PG fragments. However, only a few PG biosynthetic enzymes are direct kinase substrates. Here, we identify the conserved ReoM protein as a novel PASTA-eSTK substrate in the Gram-positive pathogen Listeria monocytogenes. Our data show that the phosphorylation of ReoM is essential as it controls ClpCP-dependent proteolytic degradation of the essential enzyme MurA, which catalyses the first committed step in PG biosynthesis. We also identify ReoY as a second novel factor required for degradation of ClpCP substrates. Collectively, our data imply that the first committed step of PG biosynthesis is activated through control of ClpCP protease activity in response to signals of PG homeostasis imbalance.

journal_name

Elife

journal_title

eLife

authors

Wamp S,Rutter ZJ,Rismondo J,Jennings CE,Möller L,Lewis RJ,Halbedel S

doi

10.7554/eLife.56048

subject

Has Abstract

pub_date

2020-05-29 00:00:00

issn

2050-084X

pii

56048

journal_volume

9

pub_type

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